Anti-PINK1 Antibody

The PTEN-induced putative kinase 1 (PINK1) is a serine/threonine protein kinase that localizes to mitochondria and is thought to protect cells from stress-induced mitochondrial dysfunction (reviewed in 1) . PINK1 recruits the E3 ubiquitin ligase Parkin to mitochondria to initiate mitophagy, an autophagic process that clears damaged mitochondria within a cell (2) . PINK1 is cleaved by the mitochondrial protease PARL (3) . Mutations in this gene cause one form of autosomal recessive early-onset Parkinson disease (4) .

PINK1 antibody is human, mouse and rat reactive. At least two isoforms are known to exist; this antibody will only detect the longer isoform. PINK1 antibody will detect the cleaved and uncleaved form of PINK1.

PINK1 antibody was raised against a 16 amino acid peptide near the amino terminus of human PINK1. The immunogen is located within amino acids 120 - 170 of PINK1.

Highly expressed in heart, skeletal muscle and testis, and at lower levels in brain, placenta, liver, kidney, pancreas, prostate, ovary and small intestine. Present in the embryonic testis from an early stage of development.

Protects against mitochondrial dysfunction during cellular stress by phosphorylating mitochondrial proteins. Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy) by mediating activation and translocation of PRKN (PubMed:14607334, PubMed:15087508, PubMed:19229105, PubMed:19966284, PubMed:20404107, PubMed:20798600, PubMed:23620051, PubMed:23754282, PubMed:23933751, PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:24896179, PubMed:25527291) . Targets PRKN to dysfunctional depolarized mitochondria through the phosphorylation of MFN2 (PubMed:23620051) . Activates PRKN in 2 steps: (1) by mediating phosphorylation at 'Ser-65' of PRKN and (2) mediating phosphorylation of ubiquitin, converting PRKN to its fully-active form (PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:25527291) . Required for ubiquinone reduction by mitochondrial complex I by mediating phosphorylation of complex I subunit NDUFA10 (By similarity) .